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Single-molecule mechanics of synthetic aromatic amide helices: Ultrafast and robust non-dissipative winding
dc.rights.license | open | en_US |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | DEVAUX, Floriane | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | LI, Xuesong | |
dc.contributor.author | SLUYSMANS, Damien | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | MAURIZOT, Victor | |
dc.contributor.author | BAKALIS, Evangelos | |
dc.contributor.author | ZERBETTO, Francesco | |
hal.structure.identifier | Chimie et Biologie des Membranes et des Nanoobjets [CBMN] | |
dc.contributor.author | HUC, Ivan | |
dc.contributor.author | DUWEZ, Anne-Sophie | |
dc.date.accessioned | 2021-07-02T06:40:44Z | |
dc.date.available | 2021-07-02T06:40:44Z | |
dc.date.issued | 2021-05 | |
dc.identifier.issn | 2451-9294 | en_US |
dc.identifier.other | https://doi.org/10.1016/j.chempr.2021.02.030 | en_US |
dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/94958 | |
dc.description.abstractEn | Because of proteins’ many degrees of conformational freedom, programming protein folding dynamics, overall elasticity, and motor functions remains an elusive objective. Instead, smaller and simpler objects, such as synthetic foldamers, may be amenable to design. However, little is known about their mechanical performance. Here, we show that reducing molecular size may not compromise mechanical properties. We report that helical aromatic oligoamides as small as 1 nm possess outstanding elasticity and outperform most natural helices. Using single-molecule force spectroscopy, we characterize their folding trajectories and intermediate states. We show that they cooperatively and reversibly unwind at high forces. They extend up to 3.8 times their original length and rewind against considerable forces on a timescale of 10 μs. Pulling and relaxing cycles follow the same trace up to a very high loading rate, indicating that the mechanical energy accumulated during the stretching does not dissipate and is immediately reusable. | |
dc.language.iso | EN | en_US |
dc.subject.en | foldamers | |
dc.subject.en | helical folding | |
dc.subject.en | AFM force spectroscopy | |
dc.subject.en | single-molecule mechanics | |
dc.subject.en | elasticity | |
dc.subject.en | reversible processes | |
dc.subject.en | molecular machines with tailored properties | |
dc.title.en | Single-molecule mechanics of synthetic aromatic amide helices: Ultrafast and robust non-dissipative winding | |
dc.type | Article de revue | en_US |
dc.identifier.doi | 10.1016/j.chempr.2021.02.030 | en_US |
dc.subject.hal | Chimie/Matériaux | en_US |
dc.description.sponsorshipEurope | Beyond Biopolymers: Protein-Sized Aromatic Amide Functional Foldamers | en_US |
dc.description.sponsorshipEurope | Erasmus Mundus - International Doctoral School in Functional Materials | en_US |
bordeaux.journal | Chem | en_US |
bordeaux.page | 1333-1346 | en_US |
bordeaux.volume | 7 | en_US |
bordeaux.hal.laboratories | Institut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248 | en_US |
bordeaux.issue | 5 | en_US |
bordeaux.institution | Université de Bordeaux | en_US |
bordeaux.institution | Bordeaux INP | en_US |
bordeaux.institution | CNRS | en_US |
bordeaux.peerReviewed | oui | en_US |
bordeaux.inpress | non | en_US |
hal.identifier | hal-03276336 | |
hal.version | 1 | |
hal.date.transferred | 2021-07-02T06:40:48Z | |
hal.export | true | |
bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Chem&rft.date=2021-05&rft.volume=7&rft.issue=5&rft.spage=1333-1346&rft.epage=1333-1346&rft.eissn=2451-9294&rft.issn=2451-9294&rft.au=DEVAUX,%20Floriane&LI,%20Xuesong&SLUYSMANS,%20Damien&MAURIZOT,%20Victor&BAKALIS,%20Evangelos&rft.genre=article |
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